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receptors (CD89) lacking 
chain association and mediate noninflammatory properties of secretory IgA
,
* Department of Immunology of Instituto de Ciências Biomédicas, and
Division of Rheumatology, University of São Paulo, SP, Brazil
Institut National de la Santé et de la Recherche Médicale, Unité 25, Hôpital Necker, Paris, France
Correspondence: R. C. Monteiro, INSERM U25, Hôpital Necker, 161, rue de Sèvres, 75743 Paris, France. E-mail: monteiro{at}necker.fr
Colostrum plays an important role in protecting newborn infants
against acute gastrointestinal and respiratory infections. IgA
antibodies have been considered the major effector component; however,
the role of their receptors on colostral phagocytes, especially
neutrophils, has not been studied. Here, we demonstrate that
CD15+ colostrum neutrophils express IgA Fc receptors
(Fc
R, CD89) at levels similar to those of blood neutrophils. Most
colostral cells (70%) bear secretory IgA (SIgA) on their surface (and
intracellularly), whereas blood cells do not. The FcR on colostral
neutrophils was identified as the a.1 isoform with a similar molecular
mass (55–75 kDa) as that identified for blood neutrophils. Removal of
N-linked carbohydrates revealed a major protein core of 32 kDa for both
cell types. In contrast, co-immunoprecipitation and immunoblot
experiments using a mild detergent, digitonin, revealed a lack of 
chain association with FcR (-less) exclusively on colostral
neutrophils. The functional role of these -less FcR cells was
evaluated by measuring superoxide release and killing of SIgA-coated
enteropathogenic E. coli. No increase in superoxide release
was observed in colostral cells compared with blood neutrophils,
whereas optimal release was obtained with PMA stimulation. Furthermore,
despite similar bacterial phagocytosis index between both cell types,
IgA-mediated bacterial-killing was not detectable with colostral
neutrophils, whereas killing was detectable on blood cells. These
results reveal exclusive expression of -less FcR on colostral
neutrophils associated with receptor hyperoccupation by IgA and with
low, bacterial-killing activity, which suggest that this receptor may
mediate noninflammatory effects of SIgA.
Key Words: human milk • IgA • EPEC • SOD • PMA
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